Protein family
Protein sequence
Protein function
Catalytic activity
EC number
EC number description
3.6.4.10
Hydrolases;
Acting on acid anhydrides;
Acting on acid anhydrides to facilitate cellular and subcellular movement;
non-chaperonin molecular chaperone ATPase
PDB | Resolution (Å) | PDB name |
---|---|---|
3IUC | 2.4 | Crystal structure of the human 70kDa heat shock protein 5 (BiP/GRP78) ATPase domain in complex with ADP |
3LDL | 2.3 | Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with ATP |
3LDN | 2.2 | Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in apo form |
3LDO | 1.95 | Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with AMPPNP |
3LDP | 2.2 | Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with small molecule inhibitor |
5E84 | 2.99 | ATP-bound state of BiP |
5E85 | 2.57 | isolated SBD of BiP |
5E86 | 2.681 | isolated SBD of BiP with loop34 modification |
5EVZ | 1.85 | Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with ADP and inorganic phosphate |
5EX5 | 1.9 | Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with 7-deaza-ADP and inorganic phosphate |
5EXW | 1.9 | Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with 7-deaza-ATP |
5EY4 | 1.86 | Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with 2'-deoxy-ATP |
5F0X | 1.6 | Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with 2'-deoxy-ADP and inorganic phosphate |
5F1X | 1.9 | Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with ATP |
5F2R | 2.15 | Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with AMP-PCP |
6ASY | 1.85 | BiP-ATP2 |
6CZ1 | 1.68 | Crystal structure of ATPase domain of Human GRP78 bound to Ver155008 |
6DFM | 2.14 | Crystal structure of human GRP78 in complex with 8-aminoadenosine |
6DFO | 2.54 | Crystal structure of human GRP78 in complex with 8-bromoadenosine |
6DO2 | 1.7 | Crystal structure of human GRP78 in complex with 7-deaza-2'-C-methyladenosine |
6DWS | 1.9 | Crystal structure of human GRP78 in complex with (2R,3R,4S,5R)-2-(6-amino-8-((2-chlorobenzyl)amino)-9H-purin-9-yl)-5-(hydroxymethyl)tetrahydrofuran-3,4-diol |
6ZMD | 2.64 | Crystal structure of HYPE covalently tethered to BiP bound to AMP-PNP |
7N1R | 2.03 | A novel and unique ATP hydrolysis to AMP by a human Hsp70 BiP |
GO ontology | GO term | GO description |
---|---|---|
Biological Process | GO:0006983 | ER overload response |
Biological Process | GO:0071236 | cellular response to antibiotic |
Biological Process | GO:0071320 | cellular response to cAMP |
Biological Process | GO:0071277 | cellular response to calcium ion |
Biological Process | GO:0071480 | cellular response to gamma radiation |
Biological Process | GO:0042149 | cellular response to glucose starvation |
Biological Process | GO:0071353 | cellular response to interleukin-4 |
Biological Process | GO:0071287 | cellular response to manganese ion |
Biological Process | GO:1990090 | cellular response to nerve growth factor stimulus |
Biological Process | GO:0071466 | cellular response to xenobiotic stimulus |
Biological Process | GO:0021680 | cerebellar Purkinje cell layer development |
Biological Process | GO:0021589 | cerebellum structural organization |
Biological Process | GO:0051085 | chaperone cofactor-dependent protein refolding |
Biological Process | GO:0030968 | endoplasmic reticulum unfolded protein response |
Biological Process | GO:0001554 | luteolysis |
Biological Process | GO:0035437 | maintenance of protein localization in endoplasmic reticulum |
Biological Process | GO:1903895 | negative regulation of IRE1-mediated unfolded protein response |
Biological Process | GO:0043066 | negative regulation of apoptotic process |
Biological Process | GO:0031333 | negative regulation of protein-containing complex assembly |
Biological Process | GO:0030512 | negative regulation of transforming growth factor beta receptor signaling pathway |
Biological Process | GO:0051402 | neuron apoptotic process |
Biological Process | GO:0030182 | neuron differentiation |
Biological Process | GO:0030335 | positive regulation of cell migration |
Biological Process | GO:0010976 | positive regulation of neuron projection development |
Biological Process | GO:0031398 | positive regulation of protein ubiquitination |
Biological Process | GO:1990440 | positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress |
Biological Process | GO:0031204 | post-translational protein targeting to membrane, translocation |
Biological Process | GO:0034975 | protein folding in endoplasmic reticulum |
Biological Process | GO:0042026 | protein refolding |
Biological Process | GO:1903891 | regulation of ATF6-mediated unfolded protein response |
Biological Process | GO:1903894 | regulation of IRE1-mediated unfolded protein response |
Biological Process | GO:1903897 | regulation of PERK-mediated unfolded protein response |
Biological Process | GO:0060904 | regulation of protein folding in endoplasmic reticulum |
Biological Process | GO:0042220 | response to cocaine |
Biological Process | GO:1904313 | response to methamphetamine hydrochloride |
Biological Process | GO:0097501 | stress response to metal ion |
Biological Process | GO:0021762 | substantia nigra development |
Biological Process | GO:1901998 | toxin transport |
Biological Process | GO:0030433 | ubiquitin-dependent ERAD pathway |
Molecular Function | GO:0005524 | ATP binding |
Molecular Function | GO:0016887 | ATP hydrolysis activity |
Molecular Function | GO:0140662 | ATP-dependent protein folding chaperone |
Molecular Function | GO:0045296 | cadherin binding |
Molecular Function | GO:0005509 | calcium ion binding |
Molecular Function | GO:0019899 | enzyme binding |
Molecular Function | GO:0031072 | heat shock protein binding |
Molecular Function | GO:0051787 | misfolded protein binding |
Molecular Function | GO:0019904 | protein domain specific binding |
Molecular Function | GO:0044183 | protein folding chaperone |
Molecular Function | GO:0051087 | protein-folding chaperone binding |
Molecular Function | GO:0043022 | ribosome binding |
Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
Molecular Function | GO:0051082 | unfolded protein binding |
Cellular Component | GO:0009986 | cell surface |
Cellular Component | GO:0005737 | cytoplasm |
Cellular Component | GO:0005829 | cytosol |
Cellular Component | GO:0005783 | endoplasmic reticulum |
Cellular Component | GO:0034663 | endoplasmic reticulum chaperone complex |
Cellular Component | GO:0005788 | endoplasmic reticulum lumen |
Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
Cellular Component | GO:0005793 | endoplasmic reticulum-Golgi intermediate compartment |
Cellular Component | GO:0070062 | extracellular exosome |
Cellular Component | GO:0005925 | focal adhesion |
Cellular Component | GO:0043231 | intracellular membrane-bounded organelle |
Cellular Component | GO:0042470 | melanosome |
Cellular Component | GO:0016020 | membrane |
Cellular Component | GO:0030496 | midbody |
Cellular Component | GO:0005739 | mitochondrion |
Cellular Component | GO:0005634 | nucleus |
Cellular Component | GO:0005886 | plasma membrane |
Cellular Component | GO:0032991 | protein-containing complex |
Cellular Component | GO:0005790 | smooth endoplasmic reticulum |
InterPro | InterPro name |
---|---|
IPR013126 | Heat shock protein 70 family |
IPR018181 | Heat shock protein 70, conserved site |
IPR029047 | Heat shock protein 70kD, peptide-binding domain superfamily |
IPR029048 | Heat shock protein 70kD, C-terminal domain superfamily |
IPR042050 | Endoplasmic reticulum chaperone BIP, nucleotide-binding domain |
IPR043129 | ATPase, nucleotide binding domain |
Pfam | Pfam name |
---|---|
PF00012 | Hsp70 protein |
Reactome | Reactome Name | Node type | Reactome Root | Reactome Root Name |
---|---|---|---|---|
R-HSA-114608 | Platelet degranulation | Leaf | R-HSA-109582 | Hemostasis |
R-HSA-3371453 | Regulation of HSF1-mediated heat shock response | Leaf | R-HSA-8953897 | Cellular responses to stimuli |
R-HSA-381033 | ATF6 (ATF6-alpha) activates chaperones | Internal node | R-HSA-8953897 | Cellular responses to stimuli |
R-HSA-381042 | PERK regulates gene expression | Internal node | R-HSA-8953897 | Cellular responses to stimuli |
R-HSA-381070 | IRE1alpha activates chaperones | Internal node | R-HSA-8953897 | Cellular responses to stimuli |
R-HSA-381183 | ATF6 (ATF6-alpha) activates chaperone genes | Leaf | R-HSA-8953897 | Cellular responses to stimuli |
R-HSA-983170 | Antigen Presentation: Folding, assembly and peptide loading of class I MHC | Leaf | R-HSA-168256 | Immune System |
Location | ECO term | Pubmed |
---|---|---|
Cell surface | ECO:0000269 | PubMed:15098107 |
Cell surface | ECO:0000269 | PubMed:20484814 |
Cell surface | ECO:0000269 | PubMed:24355926 |
Cell surface | ECO:0000269 | PubMed:27159390 |
Cell surface | ECO:0000269 | PubMed:28053106 |
Cell surface | ECO:0000269 | PubMed:33432092 |
Cytoplasm | ECO:0000250 | |
Endoplasmic reticulum lumen | ECO:0000269 | PubMed:21080038 |
Endoplasmic reticulum lumen | ECO:0000269 | PubMed:21289099 |
Endoplasmic reticulum lumen | ECO:0000269 | PubMed:23990668 |
Endoplasmic reticulum lumen | ECO:0000269 | PubMed:29497057 |
Melanosome | ECO:0000269 | PubMed:12643545 |